Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family

R. M. Ten, L. R. Pease, D. J. McKean, M. P. Bell, G. J. Gleich

Research output: Contribution to journalArticlepeer-review

165 Scopus citations

Abstract

Human eosinophil peroxidase (EPO) was purified from eosinophil granules derived from the peripheral blood of patients with eosinophilia. The molecular mass of the H and L subunits was determined by gel filtration to be 57,000 and 11,000 daltons, respectively. The partial amino acid sequences of both subunits were used to construct oligonucleotides for the screening of several cDNA libraries, including one derived from human-induced umbilical cord mononuclear cells. A cDNA clone was isolated corresponding to EPO. The nucleotide sequence revealed an open reading frame of 2,106 bp, corresponding to a prosequence, L chain, and H chain, in this order. Comparison of the EPO nucleotide sequence with other peroxidases, such as myeloperoxidase, suggests the existence of a multigene family.

Original languageEnglish (US)
Pages (from-to)1757-1769
Number of pages13
JournalJournal of Experimental Medicine
Volume169
Issue number5
DOIs
StatePublished - 1989

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint Dive into the research topics of 'Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family'. Together they form a unique fingerprint.

Cite this